@article {70371,
	title = {Molecular architecture of the fungal-specific potassium channel TOK1},
	journal = {Nat Commun},
	year = {2026},
	month = {2026 Apr 27},
	abstract = {<p>In Candida albicans, potassium (K) channels fine-tune ionic balance under stress, contributing to host colonization. Fungal two-pore domain, outwardly rectifying potassium (TOK) channels remain insufficiently characterized despite evidence implicating them in growth and viability. Here, we describe the atomic-resolution structure of a fungal potassium channel, TOK1 from C. albicans (CaTOK), revealing an architecture defined by eight transmembrane helices and a membrane topology distinct from previously characterized K$^{+}$ channel classes. The first four helices form a tetraspanin-like bundle resembling auxiliary subunits of human neuronal ion channels. The pore features an inner helical gating movement analogous to mammalian dimeric K channels, while the K selectivity filter exhibits atypical ion coordination. A cytosolic C-terminal bundle forms an intramolecular network that likely stabilizes CaTOK and may mediate gating. These findings provide a framework for understanding TOK channel function and facilitate future studies of fungal ion homeostasis, pathogenicity, and therapeutic development.</p>
},
	issn = {2041-1723},
	doi = {10.1038/s41467-026-72232-y},
	url = {https://doi.org/10.1038/s41467-026-72232-y},
	author = {Durocher, Brice and Manville, R{\'\i}an W and Yan, Rui and Yu, Zhiheng and Abbott, Geoffrey W and Miller, Alexandria N}
}
